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Database: UniProt
Entry: A0A8C4X7P7_ERPCA
LinkDB: A0A8C4X7P7_ERPCA
Original site: A0A8C4X7P7_ERPCA 
ID   A0A8C4X7P7_ERPCA        Unreviewed;       994 AA.
AC   A0A8C4X7P7;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=FLT3 {ECO:0000313|Ensembl:ENSECRP00000011633.1};
OS   Erpetoichthys calabaricus (Rope fish) (Calamoichthys calabaricus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Polypteriformes; Polypteridae; Erpetoichthys.
OX   NCBI_TaxID=27687 {ECO:0000313|Ensembl:ENSECRP00000011633.1, ECO:0000313|Proteomes:UP000694620};
RN   [1] {ECO:0000313|Ensembl:ENSECRP00000011633.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Wellcome Sanger Institute Data Sharing;
RL   Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSECRP00000011633.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSECRP00000011633.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00051243};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
CC       protein {ECO:0000256|RuleBase:RU000311}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. CSF-1/PDGF receptor subfamily.
CC       {ECO:0000256|RuleBase:RU000311}.
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DR   RefSeq; XP_028655320.1; XM_028799487.2.
DR   AlphaFoldDB; A0A8C4X7P7; -.
DR   Ensembl; ENSECRT00000011824.1; ENSECRP00000011633.1; ENSECRG00000007743.1.
DR   GeneID; 114650051; -.
DR   GeneTree; ENSGT00940000160575; -.
DR   OrthoDB; 3256376at2759; -.
DR   Proteomes; UP000694620; Chromosome 4.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019838; F:growth factor binding; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030183; P:B cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:TreeGrafter.
DR   FunFam; 1.10.510.10:FF:000426; Receptor-type tyrosine-protein kinase FLT3; 1.
DR   FunFam; 3.30.200.20:FF:000366; receptor-type tyrosine-protein kinase FLT3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR050122; RTK.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR   PANTHER; PTHR24416:SF356; RECEPTOR-TYPE TYROSINE-PROTEIN KINASE FLT3; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF25305; Ig_PDGFR_d4; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000615-
KW   2}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW   ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000615-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694620};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000311};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        547..568
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          171..344
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          614..965
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        828
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         593
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         621..628
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         832
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         833
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         846
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   SITE            972
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ   SEQUENCE   994 AA;  113893 MW;  8D2518F5B47BB7C9 CRC64;
     MEFKKGNTRN SKYFLVAAYL VISTKMYVFQ ADTSVQCFMI SHMQKTKPDL IQRQQAANRS
     VELVNISCSL MKSIGNDETE IGKKFSEIEL DFLDTVEIQA TLNGFESVNC SWKHRDAISG
     CITDKSRTTF SFMIIEADKK QAGQYLLLFQ TPNSSFLVEF RVQVLTYPMK PLLRVYERKD
     GYSLIVQCTS EGYPPPSIDW LSDDTPDDKC AKSDDKTQTV DYSGMVVKNI SGSQIHKEMK
     WCCACNRLGM ECSRLIDLGQ LLERFESEPR VFLKVGDPFL FRCSDYNNFP IIRSDHTEKK
     LHFIEEHYGK KKIRYIAFQS VAMEDSGLYT CLLSGNKSRS LMLSVVEKGF LNFSKIIRQN
     EITPPNSICL NVTVFAFPPI QCKWMYNKEL FSCNVQEPAY ETRRTFIFCH HHNIPGTYVF
     LGGNQEFKVR EQLDLYVKAT PHISLAFETD GKVACIGESY PEPALTWLEC PEELNCSGET
     SWKKINDNGI ASVTDGQIFG HKKVSNLLDL NSLSKKHWIR CCAQNDYGSF CQNVGQANLP
     QKSEKTLYYA TVGVGVPVVI LLLCFMYYNG KRKPKYENQM QMIQFIGPSD NEYIYIDFRN
     IEYDTKWEFP RENLKLGKEL GAGAFGKVVA ANAFGIFKPG ESLQVAVKML KDKYQPSEKD
     AIMAELKMLT QIGNHENIVN LLGACTVSGP VYLIFQYCQN GDLLNYLRSN RDKFQKTLAI
     VLTQNSLSLY HNIQQDHILS NGNFQHDGSY IPMHPINMVK TLEGERETLL NTSNFEDCKT
     FHGCDYKNVK IYQERELQVL TFEDLLSFSH QVAKGMEFLT SKNCIHRDLA ARNVLVTHGK
     TAKIADFGLA RDIMNDSNYV VKGNARLPVK WMPPESLFEG MYTFQSDVWS YGILLWEIFS
     LGVNPYPGIQ VDQNFYKLIQ NGFKMDQPFY ATERIYTMMK SCWALEARKR PGFSHIVSFM
     ESELMEAEEE LYHNSRCRNN QSFVAKAHQK SPSL
//
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